ID S7NMX4_MYOBR Unreviewed; 986 AA.
AC S7NMX4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=D623_10019858 {ECO:0000313|EMBL:EPQ18974.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18974.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR EMBL; KE164590; EPQ18974.1; -; Genomic_DNA.
DR RefSeq; XP_005884337.1; XM_005884275.2.
DR AlphaFoldDB; S7NMX4; -.
DR GeneID; 102239903; -.
DR KEGG; myb:102239903; -.
DR CTD; 9400; -.
DR eggNOG; KOG0352; Eukaryota.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd18014; DEXHc_RecQ5; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 6.10.250.2460; -; 1.
DR Gene3D; 6.10.250.3140; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010716; RECQ5.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF159; ATP-DEPENDENT DNA HELICASE Q5; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF06959; RecQ5; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 38..212
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 240..398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 107240 MW; ABD78EC399472BB9 CRC64;
MSTHRSSPFD PERRVRSTLK KVFGFDSFKT PLQESATMAV VKGDKDVFVC MPTGAGKSLC
YQLPALLAKG ITVVISPLIA LIQDQVDHLL ALKVQVRSLN SKLSAQEKKE LLSDLEQEKP
RTKLLYITPE MAASASFQPT LNSLVSRHLL SYLVVDEAHC VSQWGHDFRP DYLRLGALRS
RLAHAPCVAL TATATPQVRE DVFAALHLKQ PVAAFKTPCF RANLFYDVQF KELLSDPYGN
LRDFCLKALG QKAGKGVLSG CGIVYCRTRE ACEQLAIELS YRGLSAKAYH AGLKASERTL
VQNEWMEEKV PVIVATISFG MGVDKANVRF VAHWNVAKSM AGYYQESGRA GRDGRPSWCR
LYYSRSDRDQ VSFLIRKEVA KLQEKRGNKA SDKAALLAFE ALVTFCEELG CRHAAIAKYF
GDAPPACTRG CDHCQNPAAV RKQLDTLERS SSWSKTCIGP SQDNGFDPEL YEGGRRGYGG
FSRYDEGSGG SGDEGRDEAH KREWNLFYQK QMSLRKGKDP KTEEFVPPDE DCPLKEASSR
KIPRLTVKAR EHCLGLLEEA LSSNCRAAGA TQGPDLQAKA VELEHEMFRN AKAANLYKAS
VLKKVAEIHR TSKDGQLYHP AGGAKSCSAQ AEPTEHDILP ASQVYSLKPK RVGAGFPKGS
IPFQTASQLM EEMRAGGQAP RPEQRGEQEP PSQPRGLQDE ESSEPVPGLR EAPGSSAHCG
GPSPEKAKGP SGGSPAAKAR ANKKQQLLAS AALKDSQNIA RFFCQRAKSP PALASAPGVE
GASPSCAGVR GPLAVAPETC TGEEDGALGR SAARPQTECT REGPSACPLR DPGPPEGQFT
PPEGTPRGKR PRPQQENPES QARKRPHPSA GASVLAEAND NILASGQSTI SRTAQGSCQL
PAPGTSLKVA ANIVVKCLTP FYKEGKFASK DLFKAFARHL SHSLAQEPSP GRSVKEEAQH
LIRQFFRGRA RCESEADWHG LCDPQR
//
